7p0h
From Proteopedia
(Difference between revisions)
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==Crystal structure of Helicobacter pylori ComF fused to an artificial alphaREP crystallization helper(named B2)== | ==Crystal structure of Helicobacter pylori ComF fused to an artificial alphaREP crystallization helper(named B2)== | ||
| - | <StructureSection load='7p0h' size='340' side='right'caption='[[7p0h]]' scene=''> | + | <StructureSection load='7p0h' size='340' side='right'caption='[[7p0h]], [[Resolution|resolution]] 2.50Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7P0H OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7P0H FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[7p0h]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7P0H OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7P0H FirstGlance]. <br> |
| - | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=7p0h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7p0h OCA], [https://pdbe.org/7p0h PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7p0h RCSB], [https://www.ebi.ac.uk/pdbsum/7p0h PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7p0h ProSAT]</span></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PRP:ALPHA-PHOSPHORIBOSYLPYROPHOSPHORIC+ACID'>PRP</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> |
| + | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=7p0h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7p0h OCA], [https://pdbe.org/7p0h PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7p0h RCSB], [https://www.ebi.ac.uk/pdbsum/7p0h PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7p0h ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The ComFC protein is essential for natural transformation, a process that plays a major role in the spread of antibiotic resistance genes and virulence factors across bacteria. However, its role remains largely unknown. Here, we show that Helicobacter pylori ComFC is involved in DNA transport through the cell membrane, and is required for the handling of the single-stranded DNA once it is delivered into the cytoplasm. The crystal structure of ComFC includes a zinc-finger motif and a putative phosphoribosyl transferase domain, both necessary for the protein's in vivo activity. Furthermore, we show that ComFC is a membrane-associated protein with affinity for single-stranded DNA. Our results suggest that ComFC provides the link between the transport of the transforming DNA into the cytoplasm and its handling by the recombination machinery. | ||
| + | |||
| + | ComFC mediates transport and handling of single-stranded DNA during natural transformation.,Damke PP, Celma L, Kondekar SM, Di Guilmi AM, Marsin S, Depagne J, Veaute X, Legrand P, Walbott H, Vercruyssen J, Guerois R, Quevillon-Cheruel S, Radicella JP Nat Commun. 2022 Apr 12;13(1):1961. doi: 10.1038/s41467-022-29494-z. PMID:35414142<ref>PMID:35414142</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 7p0h" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Celma L]] | + | [[Category: Celma, L]] |
| - | [[Category: Legrand P]] | + | [[Category: Legrand, P]] |
| - | [[Category: Quevillon-Cheruel S]] | + | [[Category: Quevillon-Cheruel, S]] |
| - | [[Category: Walbott H]] | + | [[Category: Walbott, H]] |
| + | [[Category: Competence protein]] | ||
| + | [[Category: Recombination]] | ||
Revision as of 11:51, 27 April 2022
Crystal structure of Helicobacter pylori ComF fused to an artificial alphaREP crystallization helper(named B2)
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